AI Article Synopsis
- - RecA protein is crucial for homologous recombination repair in bacteria, forming long helical filaments on single-stranded DNA (ssDNA) when activated by ATP.
- - RecX acts as a negative regulator of RecA by promoting the disassembly of RecA-ssDNA filaments, particularly binding to the inactive form and preventing its transition to an active state.
- - This research offers new insights into how RecX interacts with RecA, emphasizing the role of conformational changes in regulating the biological activity of RecA filaments.
Article Abstract
RecA protein mediates homologous recombination repair in bacteria through assembly of long helical filaments on ssDNA in an ATP-dependent manner. RecX, an important negative regulator of RecA, is known to inhibit RecA activity by stimulating the disassembly of RecA nucleoprotein filaments. Here we use a single-molecule approach to address the regulation of () RecA-ssDNA filaments by RecX () within the framework of distinct conformational states of RecA-ssDNA filament. Our findings revealed that RecX effectively binds the inactive conformation of RecA-ssDNA filaments and slows down the transition to the active state. Results of this work provide new mechanistic insights into the RecX-RecA interactions and highlight the importance of conformational transitions of RecA filaments as an additional level of regulation of its biological activity.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9252578 | PMC |
| http://dx.doi.org/10.7554/eLife.78409 | DOI Listing |
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